Document Detail

Arrestin interaction with E3 ubiquitin ligases and deubiquitinases: functional and therapeutic implications.
MedLine Citation:
PMID:  24292831     Owner:  NLM     Status:  MEDLINE    
Arrestins constitute a small family of four homologous adaptor proteins (arrestins 1-4), which were originally identified as inhibitors of signal transduction elicited by the seven-transmembrane G protein-coupled receptors. Currently arrestins (especially arrestin2 and arrestin3; also called β-arrestin1 and β-arrestin2) are known to be activators of cell signaling and modulators of endocytic trafficking. Arrestins mediate these effects by binding to not only diverse cell-surface receptors but also by associating with a variety of critical signaling molecules in different intracellular compartments. Thus, the functions of arrestins are multifaceted and demand interactions with a host of proteins and require an array of selective conformations. Furthermore, receptor ligands that specifically induce signaling via arrestins are being discovered and their physiological roles are emerging. Recent evidence suggests that the activity of arrestin is regulated in space and time by virtue of its dynamic association with specific enzymes of the ubiquitination pathway. Ubiquitin-dependent, arrestin-mediated signaling could serve as a potential platform for developing novel therapeutic strategies to target transmembrane signaling and physiological responses.
Sudha K Shenoy
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Handbook of experimental pharmacology     Volume:  219     ISSN:  0171-2004     ISO Abbreviation:  Handb Exp Pharmacol     Publication Date:  2014  
Date Detail:
Created Date:  2013-12-02     Completed Date:  2014-04-18     Revised Date:  2014-05-12    
Medline Journal Info:
Nlm Unique ID:  7902231     Medline TA:  Handb Exp Pharmacol     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  187-203     Citation Subset:  IM    
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MeSH Terms
Arrestins / metabolism*
Drug Design
Molecular Targeted Therapy
Signal Transduction / physiology
Ubiquitin-Protein Ligases / metabolism*
Ubiquitin-Specific Proteases / metabolism*
Grant Support
Reg. No./Substance:
0/Arrestins; 0/Ligands; EC 3.4.99-/Ubiquitin-Specific Proteases; EC Ligases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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